Research workbench
AlphaFold monomer V2.0 prediction for ig mu chain C region membrane- bound form (P23735)
Analyse AlphaFold monomer V2.0 prediction for ig mu chain C region membrane- bound form… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P23735
- Type
- protein
- Length
- 380 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x661f92Fc5950020C7aB410B5F5b9a3f429F49Ae5
- Molecule
- Ig mu chain C region membrane-bound form
- UniProt
- P23735
- Pockets
- 3 · best druggability 0.51
Structure
1 distinct chain · 14% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ig mu chain C region membrane-bound form | protein | 380 | 14% helix, 44% strand | P23735 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 315 | 0.51 | 0.73 | 40 | empty |
| 2 | 145 | 0.40 | 0.73 | 23 | empty |
| 3 | 57 | 0.34 | 0.78 | 18 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P23735
- Elsewhere: UniProt P23735 · AlphaFold DB P23735
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